Substitutions in an active site loop of Escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo.
D000409:Alanine / Q000737:chemistry; D000595:Amino Acid Sequence; D001665:Binding Sites; D015153:Blotting, Western; D013437:Carbon-Sulfur Lyases / Q000737:chemistry* / Q000235:genetics; D002455:Cell Division; D002851:Chromatography, High Pressure Liquid; D003545:Cysteine / Q000737:chemistry; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry; D006836:Hydro-Lyases / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009154:Mutation; D010641:Phenotype; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012343:RNA, Transfer / Q000378:metabolism; D013347:Subcellular Fractions / Q000378:metabolism; D013385:Succinate Dehydrogenase / Q000737:chemistry; D013873:Thionucleotides / Q000096:biosynthesis*
D029968:Escherichia coli Proteins; D007506:Iron-Sulfur Proteins; C411665:IscU protein, E coli; D013873:Thionucleotides; D012343:RNA, Transfer; D013385:Succinate Dehydrogenase; D006836:Hydro-Lyases; C022362:phosphogluconate dehydratase; D013437:Carbon-Sulfur Lyases; C080546:cysteine desulfurase; D003545:Cysteine; D000409:Alanine